Cover legend: K-Cl cotransporters (KCCs) control transmembrane electrolyte flux in a variety of physiologic settings, including the acute response to altered extracellular osmolarity. In this issue of Cell, Rinehart et al. (pp. 525–536) use targeted phosphoproteomics to reveal how phosphorylation at two conserved sites in KCCs controls their activity. The image depicts the activation of KCC3 in red blood cells in response to extracellular hypotonicity. KCC3 (blue) is shown embedded in the red blood cell membrane. Cotransporters that are phosphorylated at T991 and T1048 in the C terminus (highlighted in a white “flash”) are inactive, while those that are dephosphorylated at these sites are active, allowing K-Cl efflux from the cell and preventing cell swelling due to influx of water. For more information see the article by Rinehart, J., Maksimova, Y.D., Tanis, J.E., Stone, K.E., Hodson, C.A., Zhang, J, Risinger, M., Pan, W., Wu, D., Colangelo, C.M., Forbush, B., Joiner, C.H., Gulcicek, E.E., Gallagher, P.G., and Lifton, R.P. (2009) Sites of regulated phosphorylation that control K-Cl cotransporter activity. Cell. 138(3):525-36. (PMCID: PMC2811214)

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